MAX (MYC associated factor X) is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1, and Myc. The homodimers and heterodimers compete for a common DNA target site (the E box), and rearrangement among these dimeric forms provides a complex system of transcriptional regulation. Activation of c-MYC is one of the most common oncogenic events in human malignancies [1, 2]. In normal cells, the Myc family of transcription factors (MYC, MYCL, and MYCN) regulates a diverse set of biological processes including DNA replication, gene transcription, and protein translation. Consequently, numerous cellular processes are regulated by Myc, including growth, proliferation, apoptosis, metabolism, differentiation, self-renewal, and angiogenesis [3, 4, 5]. In malignant cells, Myc activation can occur through several mechanisms such as point mutation, somatic gene amplification, chromosomal translocation, overexpression, enhanced translation, and increased protein stability [2]. The report that the inhibition of Myc in vivo had eradicated lung cancer in mice [6] suggests that Myc may be a promising therapeutic target in treating cancer. However, the Myc protein is difficult to target using small molecule probes due to its disordered conformational structure and the difficulty of finding specific probes. Since Myc and MAX dimerize in order to bind DNA and initiate transcription, Myc can be indirectly targeted by using compounds that bind MAX. If these compounds reduce Myc transcriptional activity in human cancers, they may also cause tumor regression. Thus, MAX binding compounds have potential in cancer treatment and may provide an indirect way of targeting of Myc in treating cancer and other proliferative diseases.